1o6t

<table><tr><td colspan='2'>[[1o6t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6T FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o6s|1o6s]], [[1o6v|1o6v]]</div></td></tr>

[[https://www.uniprot.org/uniprot/INLA_LISMO INLA_LISMO]] Mediates the entry of L.monocytogenes into cells.

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== Publication Abstract from PubMed ==

Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system.

Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin.,Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW Cell. 2002 Dec 13;111(6):825-36. PMID:12526809<ref>PMID:12526809</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1o6t" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Lismo]]

[[Category: Beier, V]]

[[Category: Chakraborty, T]]

[[Category: Domann, E]]

[[Category: Heinz, D W]]

[[Category: Machner, M P]]

[[Category: Schubert, W D]]

[[Category: Urbanke, C]]

[[Category: Wehland, J]]

[[Category: Ziehm, T]]

[[Category: Leucine rich repeat]]